http://purl.uniprot.org/citations/20736310 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20736310 | http://www.w3.org/2000/01/rdf-schema#comment | "The mucolipin (TRPML) subfamily of transient receptor potential (TRP) cation channels consists of three members that play various roles in the regulation of membrane and protein sorting along endo-lysosomal pathways. Loss-of-function mutations in TRPML1 cause the neurodegenerative lysosomal storage disorder, mucolipidosis type IV (MLIV), whereas a gain-of-function mutation in TRPML3 is principally implicated in the hearing-impaired and abnormally pigmented varitint-waddler mouse. Currently, TRPML2 is not implicated in any pathological disorder, but we have recently shown that it is a functional cation channel that physically interacts with TRPML1 and TRPML3 to potentially regulate lysosomal integrity. Here, we show that mutant TRPMLs heteromultimerize with other mutant and wild-type TRPMLs to regulate cell viability and starvation-induced autophagy, a process that mediates macromolecular and organellar turnover under cell starvation conditions. Heteromultimerization of dominant-negative TRPMLs with constitutively active TRPMLs rescues cells from the cytotoxic effects of TRPML constitutive activity. Moreover, dominant-negative TRPML1 channels, including a mutant channel directly implicated in MLIV pathology, also inhibit starvation-induced autophagy by interacting with and affecting native TRPML channel function. Collectively, our results indicate that heteromultimerization of TRPML channels plays a role in various TRPML-regulated mechanisms."xsd:string |
http://purl.uniprot.org/citations/20736310 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.067330"xsd:string |
http://purl.uniprot.org/citations/20736310 | http://purl.uniprot.org/core/author | "Lev S."xsd:string |
http://purl.uniprot.org/citations/20736310 | http://purl.uniprot.org/core/author | "Bach G."xsd:string |
http://purl.uniprot.org/citations/20736310 | http://purl.uniprot.org/core/author | "Frumkin A."xsd:string |
http://purl.uniprot.org/citations/20736310 | http://purl.uniprot.org/core/author | "Minke B."xsd:string |
http://purl.uniprot.org/citations/20736310 | http://purl.uniprot.org/core/author | "Zeevi D.A."xsd:string |
http://purl.uniprot.org/citations/20736310 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20736310 | http://purl.uniprot.org/core/name | "J Cell Sci"xsd:string |
http://purl.uniprot.org/citations/20736310 | http://purl.uniprot.org/core/pages | "3112-3124"xsd:string |
http://purl.uniprot.org/citations/20736310 | http://purl.uniprot.org/core/title | "Heteromultimeric TRPML channel assemblies play a crucial role in the regulation of cell viability models and starvation-induced autophagy."xsd:string |
http://purl.uniprot.org/citations/20736310 | http://purl.uniprot.org/core/volume | "123"xsd:string |
http://purl.uniprot.org/citations/20736310 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20736310 |
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